US20060205929A1 - Protein extraction from canola oil seed meal - Google Patents

Protein extraction from canola oil seed meal Download PDF

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US20060205929A1
US20060205929A1 US10/517,277 US51727703A US2006205929A1 US 20060205929 A1 US20060205929 A1 US 20060205929A1 US 51727703 A US51727703 A US 51727703A US 2006205929 A1 US2006205929 A1 US 2006205929A1
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protein
oil seed
seed meal
solution
aqueous
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Radka Milanova
E. Murray
Paul Westdal
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Burcon Nutrascience MB Corp
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Burcon Nutrascience MB Corp
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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A23J1/142—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds by extracting with organic solvents
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A23J1/142—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds by extracting with organic solvents
    • A23J1/144—Desolventization
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/14—Vegetable proteins
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants

Definitions

  • the present invention is concerned with the recovery of protein from oil seed proteins, particularly canola oil seed protein.
  • Canola oil seed is extensively processed for the recovery of canola oil therefrom.
  • the canola oil seed is crushed to remove most of the oil and the residual meal is hot solvent extracted, generally using hexane, to recover the remainder of the oil.
  • the residual meal from the solvent extraction contains residual hexane and is commonly known as “white flake” or less commonly as “marc” meal.
  • the solvent is recovered from the meal for reuse before the oil seed meal is disposed of by the crusher.
  • the oil seed meal often is heated to a higher temperature of about 120° to 140° C. in a procedure termed “toasting”.
  • the resulting meal is referred to as “toasted meal” or “high temperature produced meal”.
  • the residual oil seed meal disposed of by the crusher contains significant quantities of protein and often is employed as animal feed. There have been prior procedures to recover the canola protein from the residual canola oil seed meal in the form of a canola protein isolate.
  • the defatted protein solution then is concentrated to increase the protein concentration while maintaining the ionic strength substantially constant, after which the concentrated protein solution may be subjected to a further fat removal step.
  • the concentrated protein solution then is diluted to cause the formation of a cloud-like mass of highly aggregated protein molecules as discrete protein droplets in micellar form.
  • the protein micelles are allowed to settle to form an aggregated, coalesced, dense, amorphous, sticky gluten-like protein isolate mass, termed “protein micellar mass” or PMM, which is separated from the residual aqueous phase and dried.
  • the protein isolate has a protein content (as determined by Kjeldahl or equivalent method N ⁇ 6.25) of at least about 90 wt %, is substantially undenatured (as determined by differential scanning calorimetry) and has a low residual fat content.
  • protein content refers to the quantity of protein in the protein isolate expressed on a dry weight basis. The yield of protein isolate obtained using this procedure, in terms of the proportion of protein extracted from the oil seed meal which is recovered as dried protein isolate was generally less than 40 wt %, typically around 20 wt %.
  • the protein isolate is made by a process in which oil seed meal is extracted with a food grade salt solution, the resulting protein solution, after an initial treatment with a colourant adsorbent, if desired, is concentrated to a protein content of at least about 200 g/L, and the concentrated protein solution is diluted in chilled water to form protein micelles, which are allowed to settle to form an aggregated, coalesced, dense amorphous, sticky gluten-like protein isolate mass, termed “protein micellar mass” or PMM, which is separated from residual aqueous phase and may be used as such or dried.
  • protein micellar mass protein micellar mass
  • the supernatant from the PMM settling step is processed to recover a protein isolate comprising dried protein from wet PMM and supernatant.
  • This procedure may be effected by initially concentrating the supernatant using ultrafiltration membranes, mixing the concentrated supernatant with the wet PMM and drying the mixture.
  • the resulting canola protein isolate has a high purity of at least about 90 wt %, preferably at least about 100 wt %, protein (N ⁇ 6.25).
  • the supernatant from the PMM settling step is processed to recover a protein from the supernatant.
  • This procedure may be effected by initially concentrating the supernatant using ultrafiltration membranes and drying the concentrate.
  • the resulting canola protein isolate has a high purity of at least about 90 wt %, preferably at least about 100 wt %, protein (N ⁇ 6.25).
  • canola oil seed meal is continuously mixed with a salt solution, the mixture is conveyed through a pipe while extracting protein from the canola oil seed meal to form an aqueous protein solution, the aqueous protein solution is continuously separated from residual canola oil seed meal, the aqueous protein solution is continuously conveyed through a selective membrane operation to increase the protein content of the aqueous protein solution to at least about 200 g/L while maintaining the ionic strength substantially constant, the resulting concentrated protein solution is continuously mixed with chilled water to cause the formation of protein micelles, and the protein micelles are continuously permitted to settle while the supernatant is continuously overflowed until the desired amount of PMM has accumulated in the settling vessel.
  • the PMM is removed from the settling vessel and may be dried.
  • the PMM has a protein content of at least about 90 wt % (N ⁇ 6.25), preferably at least about 100 wt %.
  • a process of preparing a protein isolate which comprises (a) crushing oil seeds to form oil and oil seed meal therefrom, (b) solvent extracting the oil seed meal to recover residual oil therefrom, (c) removing solvent from the extracted oil seed meal at a temperature of below about 50° C.
  • the present invention uses white flake or marc meal which has been desolventized at moderate temperatures below about 50° C., preferably at about 15° to about 30° C.
  • Desolventizing may be effected by air drying the meal or by vacuum stripping.
  • the protein may be extracted and recovered from the ambient temperature desolventized meal by either a batch process, a semi-batch process or a continuous process as generally described in the aforementioned U.S. patent applications.
  • the protein isolate produced according to the process herein may be used in conventional applications of protein isolates, such as, protein fortification of processed foods, emulsification of oils, body formers in baked goods and foaming agents in products which entrap gases.
  • the protein isolate may be formed into protein fibers, useful in meat analogs, may be used as an egg white substitute or extender in food products where egg white is used as a binder.
  • the canola protein isolate may be used as nutritional supplements. Other uses of the canola protein isolate are in pet foods, animal feed and in industrial and cosmetic applications and in personal care products.
  • FIGS. 1 to 3 are HPLC chromatograms of extractions of canola oil seed meal which has been air-desolventized meal at room temperature using 0.05 M NaCl ( FIG. 1 ) and 0.10 M NaCl ( FIG. 2 ) and at 60° C. in the absence of salt ( FIG. 3 ).
  • the process of the invention commences with oil seed, particularly canola oil seed, although the process may be applied to other oil seeds, such as soybean, traditional rapeseed, traditional flax, linola, sunflower and mustard oil seed meals.
  • oil seed particularly canola oil seed
  • the process may be applied to other oil seeds, such as soybean, traditional rapeseed, traditional flax, linola, sunflower and mustard oil seed meals.
  • the invention is more particularly described herein with respect to canola oil seed meal.
  • the oil seed is washed to recover oil therefrom.
  • the residual meal is solvent extracted, usually using hexane, to recover residual amounts of oil from the meal.
  • the resulting meal then is desolventized in accordance with the present invention at a temperature below about 50° C., preferably at about 15° to about 30° C. By effecting desolventizing in this manner, it has been found that the amount of protein which can be extracted from the meal is significantly increased.
  • the oil seed meal which is processed in this manner may be processed as described in the Murray I or II patents to recover protein isolate from the oil seed meal, details of which are described therein.
  • 10/137,391 (WO 02/089567) is employed since there are obtained thereby improved yields of dried protein isolate, in terms of the proportion of the protein extracted from the oil seed meal which is recovered as protein isolate and a protein isolate of high protein content is obtained, usually at least about 100 wt % as determined by the Kjeldahl method as percent nitrogen (N) and multiplied by a factor of 6.25.
  • N percent nitrogen
  • the continuous process described in the aforementioned U.S. Applications Nos. 60/331,646, 60/383,809 and Ser. No. 10/298,678 may be employed. Details of these preferred procedures as applied to canola protein isolate are described below.
  • processing of the oil seed to recover oil therefrom may be effected in a different facility from that at which the protein isolate is recovered from the oil seed meal. Alternatively, the operations may be combined at a single facility.
  • the initial step of the process of separating the canola protein isolate involves solubilizing proteinaceous material from canola oil seed meal.
  • the proteinaceous material recovered from canola seed meal may be the protein naturally occurring in canola seed or other oil seed or the proteinaceous material may be a protein modified by genetic manipulation but possessing characteristic hydrophobic and polar properties of the natural protein.
  • Canola oil seed is also known as rapeseed or oil seed rape.
  • Protein solubilization is effected most efficiently by using a food grade salt solution since the presence of the salt enhances the removal of soluble protein from the oil seed meal.
  • non-food grade chemicals may be employed.
  • the food grade salt usually is sodium chloride, although other salts, such as, potassium chloride, may be used.
  • the food grade salt solution has an ionic strength of at least about 0.10, preferably at least about 0.15, to enable solubilization of significant quantities of protein to be effected. As the ionic strength of the salt solution increases, the degree of solubilization of protein in the oil seed meal initially increases until a maximum value is achieved. Any subsequent increase in ionic strength does not increase the total protein solubilized.
  • the ionic strength of the food grade salt solution which causes maximum protein solubilization varies depending on the salt concerned and the oil seed meal chosen.
  • an ionic strength value less than about 0.8, and more preferably a value of about 0.15 to about 0.6.
  • the salt solubilization of the protein is effected at a temperature of at least about 5° and preferably up to about 35° C., preferably accompanied by agitation to decrease the solubilization time, which is usually about 10 to about 60 minutes. It is preferred to effect the solubilization to extract substantially the maximum amount of protein from the oil seed meal, so as to provide an overall high product yield.
  • the lower temperature limit of about 5° C. is chosen since solubilization is impractically slow below this temperature while the upper preferred temperature limit of about 35° C. is chosen since the process becomes uneconomic at higher temperature levels in a batch mode.
  • the extraction of the protein from the canola oil seed meal is carried out in any manner consistent with effecting a continuous extraction of protein from the canola oil seed meal.
  • the canola oil seed meal is continuously mixed with a salt solution and the mixture is conveyed through a pipe or conduit having a length and at a flow rate for a residence time sufficient to effect the desired extraction in accordance with the parameters described herein.
  • the salt solubilization step is effected rapidly, in a time of up to about 10 minutes, preferably to effect solubilization to extract substantially the maximum amount of protein from the canola oil seed meal.
  • the solubilization in the continuous procedure preferably is effected at elevated temperatures, preferably above about 35° C., generally up to about 65° C. or more.
  • the aqueous food grade salt solution and the canola oil seed meal have a natural pH of about 5 to about 6.8 to enable a protein isolate to be formed by the micellar route, as described in more detail below.
  • pH values of about 5.3 to about 6.2 are preferred.
  • the pH of the food grade salt solution may be adjusted to any desired value within the range of about 5 to about 6.8 for use in the extraction step by the use of any convenient food grade acid, usually hydrochloric acid, or food grade alkali, usually sodium hydroxide, as required. Where the canola protein isolate is intended for non-food uses, then non-food grade chemicals may be used.
  • concentration of oil seed meal in the food grade salt solution during the solubilization step may vary widely. Typical concentration values are about 5 to about 15% w/v.
  • the protein extraction step with the aqueous salt solution has the additional effect of solubilizing fats which may be present in the canola meal, which then results in the fats being present in the aqueous phase.
  • the protein solution resulting from the extraction step generally has a protein concentration of about 5 to about 40 g/L, preferably about 10 to about 30 g/L.
  • the aqueous phase resulting from the extraction step then may be separated from the residual canola meal, in any convenient manner, such as by employing vacuum filtration, followed by centrifugation and/or filtration to remove residual meal.
  • the separated residual meal may be dried for disposal.
  • the colour of the final canola protein isolate can be improved to obtain a lighter and less intense yellow colour by the mixing of powdered activated carbon or other pigment adsorbing agent with the separated aqueous protein solution and subsequently removing the adsorbent, conveniently by filtration, to provide a protein solution. Diafiltration of the separated aqueous protein solution, before or after concentration, as described below, also may be used for pigment removal.
  • Such pigment removal step may be carried out under any convenient conditions, generally at the ambient temperature of the separated aqueous protein solution, employing any suitable pigment adsorbing agent.
  • any suitable pigment adsorbing agent for powdered activated carbon, an amount of about 0.025% to about 5% w/v, preferably about 0.05% to about 2% w/v, is employed.
  • the defatting steps described therein may be effected on the separated aqueous protein solution and on the concentrated aqueous protein solution discussed below.
  • the colour improvement step may be effected after the first defatting step.
  • such extraction may be made using water alone, although the utilization of water alone tends to extract less protein from the oil seed meal than the aqueous food grade salt solution.
  • the food grade salt in the concentrations discussed above, may be added to the protein solution after separation from the residual oil seed meal in order to maintain the protein in solution during the concentration step described below.
  • the food grade salt generally is added after completion of such operations.
  • Another alternative procedure is to extract the oil seed meal with the food grade salt solution at a relatively high pH value above about 6.8, generally up to about 9.8.
  • the pH of the food grade salt solution may be adjusted in pH to the alkaline value by the use of any convenient food-grade alkali, such as aqueous sodium hydroxide solution.
  • the aqueous phase resulting from the oil seed meal extraction step then is separated from the residual canola meal, in any convenient manner, such as by employing vacuum filtration, followed by centrifugation and/or filtration to remove residual meal.
  • the separated residual meal may be dried for disposal.
  • the aqueous protein solution resulting from the high pH extraction step then is pH adjusted to the range of about 5 to about 6.8, preferably about 5.3 to about 6.2, as discussed above, prior to further processing as discussed below.
  • pH adjustment may be effected using any convenient food grade acid, such as hydrochloric acid.
  • the aqueous protein solution then is concentrated to increase the protein concentration thereof while maintaining the ionic strength thereof substantially constant.
  • concentration generally is effected to provide a concentrated protein solution having a protein concentration of at least about 200 g/L, preferably at least about 250 g/L.
  • the concentration step may be effected in any convenient manner consistent with batch or continuous operation, such as by employing any convenient selective membrane technique, such as ultrafiltration or diafiltration, using membranes, such as hollow-fibre membranes or spiral-wound membranes, with a suitable molecular weight cut-off, such as about 3000 to about 50,000 daltons, having regard to differing membrane materials and configurations, and, for continuous operation, dimensioned to permit the desired degree of concentration as the aqueous protein solution passes through the membranes.
  • any convenient selective membrane technique such as ultrafiltration or diafiltration
  • membranes such as hollow-fibre membranes or spiral-wound membranes
  • a suitable molecular weight cut-off such as about 3000 to about 50,000 daltons
  • the concentration step may be effected at any convenient temperature, generally about 20° to about 60° C., and for the period of time to effect the desired degree of concentration.
  • the temperature and other conditions used to some degree depend upon the membrane equipment used to effect the concentration and the desired protein concentration of the solution.
  • the concentrating of the protein solution to a concentration above about 200 g/L in this step not only increases the process yield to levels above about 40% in terms of the proportion of extracted protein which is recovered as dried protein isolate, preferably above about 80%, but also decreases the salt concentration of the final protein isolate after drying.
  • the ability to control the salt concentration of the isolate is important in applications of the isolate where variations in salt concentrations affect the functional and sensory properties in a specific food application
  • the low molecular weight species include not only the ionic species of the food grade salt but also low molecular weight materials extracted from the source material, such as, carbohydrates, pigments and anti-nutritional factors, as well as any low molecular weight forms of the protein.
  • the molecular weight cut-off of the membrane is usually chosen to ensure retention of a significant proportion of the protein in the solution, while permitting contaminants to pass through having regard to the different membrane materials and configurations.
  • the concentrated protein solution may be warmed to a temperature of at least about 200, and up to about 60° C., preferably about 25° to about 40° C., to decrease the viscosity of the concentrated protein solution to facilitate performance of the subsequent dilution step and micelle formation.
  • the concentrated protein solution should not be heated beyond a temperature above which the temperature of the concentrated protein solution does not permit micelle formation on dilution by chilled water.
  • the concentrated protein solution may be subject to a farther defatting operation, if required, as described in the aforementioned U.S. Pat. Nos. 5,844,086 and 6,005,076.
  • the concentrated protein solution resulting from the concentration step and optional defatting step then is diluted to effect micelle formation by mixing the concentrated protein solution with chilled water having the volume required to achieve the degree of dilution desired.
  • the degree of dilution of the concentrated protein solution may be varied. With higher dilution levels, in general, a greater proportion of the canola protein remains in the aqueous phase.
  • the concentrated protein solution is diluted by about 15 fold or less, preferably about 10 fold or less.
  • the chilled water with which the concentrated protein solution is mixed has a temperature of less than about 15° C., generally about 3° to about 15° C., preferably less than about 10° C., since improved yields of protein isolate in the form of protein micellar mass are attained with these colder temperatures at the dilution factors used.
  • the batch of concentrated protein solution is added to a static body of chilled water having the desired volume, as discussed above.
  • the dilution of the concentrated protein solution and consequential decrease in ionic strength causes the formation of a cloud-like mass of highly associated protein molecules in the form of discrete protein droplets in micellar form.
  • the protein micelles are allowed to settle in the body of chilled water to form an aggregated, coalesced, dense, amorphous sticky gluten-like protein micellar mass PMM.
  • the settling may be assisted, such as by centrifugation.
  • Such induced settling decreases the liquid content of the protein micellar mass, thereby decreasing the moisture content generally from about 70% by weight to about 95% by weight to a value of generally about 50% by weight to about 80% by weight of the total micellar mass. Decreasing the moisture content of the micellar mass in this way also decreases the occluded salt content of the micellar mass, and hence the salt content of dried isolate.
  • the dilution operation may be carried out continuously by continuously passing the concentrated protein solution to one inlet of a T-shaped pipe, while the diluting water is fed to the other inlet of the T-shaped pipe, permitting mixing in the pipe.
  • the diluting water is fed into the T-shaped pipe at a rate sufficient to achieve the desired degree of dilution.
  • the mixing of the concentrated protein solution and the diluting water in the pipe initiates the formation of protein micelles and the mixture is continuously fed from the outlet from the T-shaped pipe into a settling vessel, from which, when full, supernatant is permitted to overflow.
  • the mixture preferably is fed into the body of liquid in the settling vessel in a manner which minimizes turbulence within the body of liquid.
  • the protein micelles are allowed to settle in the settling vessel to form an aggregated, coalesced, dense, amorphous, sticky, gluten-like protein micellar mass (PMM) and the procedure is continued until a desired quantity of the PMM has accumulated in the bottom of the settling vessel, whereupon the accumulated PMM is removed from the settling vessel.
  • PMM gluten-like protein micellar mass
  • the settled isolate is separated from the residual aqueous phase or supernatant, by such methods as decantation of the residual aqueous phase from the settled mass or centrifugation.
  • the PMM may be used in the wet form or may be dried, by any convenient technique, such as spray drying, freeze drying or vacuum drum drying, to a dry form.
  • the dry PMM has a high protein content, in excess of about 90 wt % protein, preferably at least about 100 wt % protein (calculated as Kjeldahl N ⁇ 6.25), and is substantially undenatured (as determined by differential scanning calorimetry).
  • the dry PMM isolated from fatty oil seed meal also has a low residual fat content, when the procedures of the aforementioned U.S. Pat. Nos. 5,844,086 and 6,005,076 are employed, which may be below about 1 wt %.
  • the supernatant from the PMM formation and settling step contains significant amounts of canola protein, not precipitated in the dilution step, and is processed to recover canola protein isolate therefrom.
  • the supernatant from the dilution step, following removal of the PMM, is concentrated to increase the protein concentration thereof.
  • concentration is effected using any convenient selective membrane technique, such as ultrafiltration, using membranes with a suitable molecular weight cut-off permitting low molecular weight species, including the food grade salt and other non-proteinaceous low molecular weight materials extracted from the protein source material, to pass through the membrane, while retaining canola protein in the solution.
  • Ultrafiltration membranes having a molecular weight cut-off of about 3000 to 10,000 daltons, having regard to differing membrane materials and configuration, may be used. Concentration of the supernatant in this way also reduces the volume of liquid required to be dried to recover the protein.
  • the supernatant generally is concentrated to a protein concentration of about 100 to about 400 g/L, preferably about 200 to about 300 g/L, prior to drying. Such concentration operation may be carried out in a batch mode or in a continuous operation, as described above for the protein solution concentration step.
  • the concentrated supernatant may be dried by any convenient technique, such as spray drying, freeze drying or vacuum drum-drying, to a dry form to provide a further canola protein isolate.
  • Such further canola protein isolate has a high protein content, in excess of about 90 wt %, preferably at least about 100 wt % protein (calculated as N ⁇ 6.25) and is substantially undenatured (as determined by differential scanning calorimetry).
  • At least a portion of the wet PMM may be combined with at least a portion of the concentrated supernatant prior to drying the combined protein streams by any convenient technique to provide a combined canola protein isolate composition according to one invention.
  • the relative proportions of the proteinaceous materials mixed together may be chosen to provide a canola protein isolate composition having a desired profile of 2S/7S/12S proteins.
  • the dried protein isolates may be combined in any desired proportions-to provide any desired specific 2S/7S/12S protein profile in the mixture.
  • the combined canola protein isolate composition has a high protein content, in excess of about 90 wt %, preferably at least about 100 wt %, (calculated as N ⁇ 6.25) and is substantially undenatured (as determined by differential scanning calorimetry).
  • the remainder of the concentrated supernatant may be dried as may any of the remainder of the PMM. Further, dried PMM and dried supernatant also may be dry mixed in any desired relative proportions, as discussed above.
  • canola protein isolates may be recovered, in the form of dried PMM, dried supernatant and dried mixtures of various proportions by weight of PMM and supernatant, generally from about 5:95 to about 95:5 by weight, which may be desirable for attaining differing functional and nutritional properties.
  • protein may be recovered from the concentrated protein solution by dialyzing the concentrated protein solution to reduce the salt content thereof.
  • the reduction of the salt content of the concentrated protein solution results in the formation of protein micelles in the dialysis tubing.
  • the protein micelles may be permitted to settle, collected and dried, as discussed above.
  • the supernatant from the protein micelle settling step may be processed, as discussed above, to recover further protein therefrom.
  • the contents of the dialysis tubing may be directly dried. The latter alternative procedure is useful where small laboratory scale quantities of protein are desired.
  • the protein extractability from the meals was determined from the protein concentration data of Table V and this data is presented in Table VI: TABLE VI Protein Extractability (wt %)* 0.05 M saline 0.10 M saline 60° C. water Ambient temperature 49.6 48.4 32.7 desolventized meal Toasted commercial meal 17.0 20.0 14.0 *Defined as percentage of the amount of protein extracted as of the total amount of protein in the meal.
  • Table VI shows that the protein extractability of the Marc meal at both salt concentrations were comparable with a 15 wt % meal and 0.15 M salt concentration at room temperature (see Table II above).
  • the protein extraction of the Marc meal at 0.05 M NaCl was comparable with that at 0.10 M NaCl.
  • the protein extractability was substantially lower at the elevated temperature than that using 0.05 and 0.10 M salt at room temperature. In all cases, however, the protein extractability and protein concentrations were significantly higher than obtained with toasted commercial meal.
  • a Varian high pressure liquid chromatography column using a 30 cm BioSep S3000 Size Exclusion Chromatography (SEC) column containing hydrophilic-bonded silica rigid support media, 5-micron diameter, 290-Angstrom pore size, capable of separating globular proteins from 5,000 to 700,000 dalton size, was run with a series of standards of protein origin to determine the residence time (RT) of each component, as measured at A280 nm, at an elution flow rate of 1.0 mL/min.
  • the BioRad standard proteins cover a range from 17,000 daltons (myoglobulin) to 670,000 daltons (thyroglobulin) with Vitamin B12 added as a low molecular mass marker at 1,350 daltons.
  • Each chromatogram showed a distinct peak representing 7S canola protein fraction and a small bump of 12S canola protein fraction.
  • the peak for the 2S canola protein fraction was present among peaks for other components of the extract.
  • the peaks in the lower molecular weight end of the chromatogram were not properly identified, but likely correspond to non-protein nitrogenous compounds, such as short peptides and free amino acids, as well as other meal components, such as phenolic compounds, glucosinolates and phytates.
  • This Example further illustrates the preparation of a canola protein isolate using air-desolventized canola oil seed meal.
  • the residual canola meal was removed and washed on a vacuum filter belt.
  • the resulting protein solution was clarified by centrifugation and filtration to produce 1270 L of a clarified protein solution having a protein content of 16.2 g/L.
  • 1270 L of the protein extract solution was reduced in volume to 71 L by concentration on an ultrafiltration system using 5000 dalton molecular weight cut-off membranes.
  • the protein extract solution then was diafiltered on a diafiltration system using 5000 dalton molecular weight cut-off membranes with 5000 L (5 retentate volumes) of 0.15 M saline solution containing 0.05 wt % ascorbic acid to a fmal volume of 31 L with a protein content of 226 g/L.
  • the retentate was pasteurized at 60° C. for 10 minutes.
  • the concentrated and diafiltered solution was divided into three batches of 30 L, 30 L and 8 L respectively.
  • a first batch at 30° C. was diluted 1:15 into 450 L of filtered water at 4° C.
  • a white cloud of protein micelles formed immediately and was allowed to settle.
  • the upper diluting water was removed. This procedure was repeated for the second and third batches.
  • the precipitated, viscous, sticky mass (PMM) was removed from the bottom of the vessel.
  • the dried protein was found to have a protein content of 102.4 wt % (N ⁇ 6.25) d.b. (Percentage nitrogen values were determined using a Leco FP 328 Nitrogen Determinator).
  • the product was given designation BW-AA020-C17-03A-C300.
  • 988 L of supernatant from the protein micelle formation were concentrated to 38 L on a ultrafiltration system using 5000 dalton molecular weight cut-off membranes.
  • the concentrated supernatant then was dilafiltered on a diafiltration system using 5000 dalton molecular weight cut-off membranes with 130 L (4 retentate volumes) of water to a final volume of 38 L with a protein content of 194 g/L.
  • the concentrated and diafiltered solution was diluted to a pumpable consistency and was then spray dried.
  • the dried protein was found to have a protein content of 97.6 wt % (N ⁇ 6.25) d.b.
  • the product was given designation BW-AA020-C17-03A-C200.
  • the present invention provides an improved process for making oil seed protein isolates from oil seed meals by using an ambient temperature desolventized meal to provide a greater degree of extraction of protein from the meal leading to economic benefits. Modifications are possible within the scope of this invention.

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US20060286281A1 (en) * 2002-10-22 2006-12-21 Shelley Hiron Canola protein isolate functionality II
US20090286961A1 (en) * 2008-05-16 2009-11-19 Bio Extraction Inc. Protein concentrates and isolates, and processes for the production thereof
US20110172395A1 (en) * 2008-07-11 2011-07-14 Martin Schweizer Soluble canola protein isolate production
US8486675B2 (en) 2009-11-11 2013-07-16 Bioexx Specialty Proteins Ltd. Protein concentrates and isolates, and processes for the production thereof from macroalgae and/or microalgae
US8623445B2 (en) 2008-05-16 2014-01-07 Bio-Extraction Inc. Protein concentrates and isolates, and processes for the production thereof
US8821955B2 (en) 2008-05-16 2014-09-02 Siebte Pmi Verwaltungs Gmbh Protein concentrates and isolates, and processes for the production thereof

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WO2004044659A2 (de) * 2002-11-13 2004-05-27 Seereal Technologies Gmbh Videohologramm und einrichtung zur rekonstruktion von videohologrammen
RU2386341C2 (ru) * 2004-02-17 2010-04-20 Баркон Ньютрасайнс (Мб) Корп. Получение изолята белка канолы и его применение в аквакультуре
CA2564400C (en) * 2004-05-07 2012-02-28 Burcon Nutrascience (Mb) Corp. Protein isolation procedures for reducing phytic acid
DE102004031647A1 (de) * 2004-06-28 2006-01-26 Fachhochschule Fulda vertreten durch den Präsidenten Proteinreiches, pflanzliches Lebensmittel und Verfahren zu seiner Herstellung
KR101321360B1 (ko) * 2005-07-01 2013-10-28 버콘 뉴트라사이언스 (엠비) 코포레이션 카놀라 단백질의 생산
US20070054031A1 (en) * 2005-09-02 2007-03-08 Keshun Liu Methods of extracting, concentrating and fractionating proteins and other chemical components
CA2645332A1 (en) 2006-03-03 2007-09-13 Specialty Protein Producers, Inc. Methods of separating fat from soy materials and compositions produced therefrom
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US20070207254A1 (en) * 2006-03-03 2007-09-06 Specialty Protein Producers, Inc. Methods of separating fat from soy materials and compositions produced therefrom
DE102007047764A1 (de) * 2007-10-04 2009-04-09 Süd-Chemie AG Entfernung unerwünschter Begleitstoffe aus Pflanzenproteinextrakten
US20100036099A1 (en) 2008-07-11 2010-02-11 Martin Schweizer Soluble canola protein isolate production ("nutratein")
PL2323499T3 (pl) 2008-08-18 2019-12-31 Burcon Nutrascience (Mb) Corp. Wytwarzanie izolatu białka canola bez obróbki cieplnej
US20110184149A1 (en) * 2008-08-18 2011-07-28 Segall Kevin I Preparation of canola protein isolate from canola oil seeds ("blendertein")
NZ591364A (en) * 2008-08-19 2013-03-28 Burcon Nutrascience Mb Corp Soluble canola protein isolate production from protein micellar mass
WO2010096943A2 (de) 2009-02-27 2010-09-02 Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. Aus rapssamen hergestelltes proteinpräparat
ES2904809T3 (es) 2009-05-14 2022-04-06 Burcon Nutrascience Mb Corp Producción de producto de proteína de canola sin tratamiento térmico (“C200CaC")
CA2767125A1 (en) * 2009-07-02 2011-01-06 Bioexx Specialty Proteins Ltd. Process for removing organic solvents from a biomass
PL2498619T3 (pl) 2009-11-11 2017-10-31 Siebte Pmi Verwaltungs Gmbh Koncentraty i izolaty białkowe, i sposoby ich wytwarzania z opiekanej mączki z nasion oleistych
US8404884B2 (en) * 2010-03-26 2013-03-26 University Of Saskatchewan Process for the extraction of macromolecules from a biomass using thin stillage
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US20060286281A1 (en) * 2002-10-22 2006-12-21 Shelley Hiron Canola protein isolate functionality II
US7989017B2 (en) * 2002-10-22 2011-08-02 Burcon Nutrascience (Mb) Corp. Canola protein isolate functionality II
US20090286961A1 (en) * 2008-05-16 2009-11-19 Bio Extraction Inc. Protein concentrates and isolates, and processes for the production thereof
US8529981B2 (en) 2008-05-16 2013-09-10 Bioexx Specialty Proteins Ltd. Protein concentrates and isolates, and processes for the production thereof
US8623445B2 (en) 2008-05-16 2014-01-07 Bio-Extraction Inc. Protein concentrates and isolates, and processes for the production thereof
US8821955B2 (en) 2008-05-16 2014-09-02 Siebte Pmi Verwaltungs Gmbh Protein concentrates and isolates, and processes for the production thereof
US20110172395A1 (en) * 2008-07-11 2011-07-14 Martin Schweizer Soluble canola protein isolate production
US8580330B2 (en) * 2008-07-11 2013-11-12 Burcon Nutrascience (Mb) Corp. Method of producing a canola protein isolate
US8486675B2 (en) 2009-11-11 2013-07-16 Bioexx Specialty Proteins Ltd. Protein concentrates and isolates, and processes for the production thereof from macroalgae and/or microalgae

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RU2005101354A (ru) 2005-09-20
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RU2361415C2 (ru) 2009-07-20
AU2003236760A1 (en) 2004-01-06
JP4383345B2 (ja) 2009-12-16
ATE406805T1 (de) 2008-09-15
PT1515614E (pt) 2008-12-16
BRPI0311991B1 (pt) 2015-03-24
US20040049013A1 (en) 2004-03-11
HK1083726A1 (en) 2006-07-14
ES2315504T3 (es) 2009-04-01
BR0311991A (pt) 2005-04-26
WO2004000031A1 (en) 2003-12-31
KR20050010937A (ko) 2005-01-28
US6992173B2 (en) 2006-01-31
AU2003236760B2 (en) 2009-01-22
DE60323368D1 (de) 2008-10-16
CN1674789A (zh) 2005-09-28
EP1515614B1 (en) 2008-09-03
DK1515614T3 (da) 2009-01-19
CN100456947C (zh) 2009-02-04
JP2005530854A (ja) 2005-10-13
EP1515614A1 (en) 2005-03-23
NZ537201A (en) 2007-06-29
KR101175167B1 (ko) 2012-08-20
MXPA04012777A (es) 2005-12-05

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